Real-time analysis of conformational control in electron transfer reactions of human cytochrome P450 reductase with cytochrome c.

ABSTRACT: Protein domain dynamics and electron transfer chemistry are often associated, but real-time analysis of domain motion in enzyme-catalysed reactions and the elucidation of mechanistic schemes that relate these motions to the reaction chemistry are major challenges for biological catalysis research. Previously we suggested that reduction of human cytochrome P450 reductase with the reducing coenzyme NADPH is accompanied by major structural re-orientation of the FMN- and FAD-binding domains through an inferred dynamic cycle of 'open' and 'closed' conformations of the enzyme (PLoS Biol, 2011, e1001222). However, these studies were restricted to stopped-flow/FRET analysis of the reductive half-reaction, and were compromised by fluorescence quenching of the acceptor by the flavin cofactors. Here

SUBMITTER: Hedison TM 

PROVIDER: S-EPMC4973710 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature